| SEP15 | |
| 15 kDa selenoprotein is a protein that in humans is encoded by the SEP15 gene. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. | |
| Function | |
| This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies in mouse suggest that this selenoprotein may have redox function and may be involved in the quality control of protein folding. | |
| Clinical significance | |
| This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers. | |
| Protein domain | |
| The protein this gene encodes for is often called Sep15 however in the case of mice, it is named SelM. This protein is a selenoprotein only found in eukaryotes. This domain has a thioredoxin-like domain and a surface accessible active site redox motif. This suggests that they function as thiol-disulfide isomerases involved in disulfide bond formation in the endoplasmic reticulum. | |
| Function | |
| Recent studies have shown in mice, where the SEP15 gene has been silenced the mice subsequently became deficient in SEP15 and were able to inhibit the development of colorectal cancer. | |
| Structure | |
| The particular structure has an alpha/beta central domain which is actually made up of three alpha helices and a mixed parallel/anti-parallel four-stranded beta-sheet. | |
| References | |
| Further reading |